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1t0u

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{{STRUCTURE_1t0u| PDB=1t0u | SCENE= }}
{{STRUCTURE_1t0u| PDB=1t0u | SCENE= }}
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'''Crystal structure of E.coli uridine phosphorylase at 2.2 A resolution (Type-A Native)'''
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===Crystal structure of E.coli uridine phosphorylase at 2.2 A resolution (Type-A Native)===
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==Overview==
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Uridine phosphorylase (UP) is a key enzyme in the pyrimidine salvage pathway that catalyses the reversible phosphorolysis of uridine to uracil and ribose 1-phosphate. Inhibiting liver UP in humans raises blood uridine levels and produces a protective effect ("uridine rescue") against the toxicity of the chemotherapeutic agent 5-fluorouracil without reducing its antitumour activity. We have investigated UP-substrate interactions by determining the crystal structures of native Escherichia coli UP (two forms), and complexes with 5-fluorouracil/ribose 1-phosphate, 2-deoxyuridine/phosphate and thymidine/phosphate. These hexameric structures confirm the overall structural similarity of UP to E.coli purine nucleoside phosphorylase (PNP) whereby, in the presence of substrate, each displays a closed conformation resulting from a concerted movement that closes the active site cleft. However, in contrast to PNP where helix segmentation is the major conformational change between the open and closed forms, in UP more extensive changes are observed. In particular a swinging movement of a flap region consisting of residues 224-234 seals the active site. This overall change in conformation results in compression of the active site cleft. Gln166 and Arg168, part of an inserted segment not seen in PNP, are key residues in the uracil binding pocket and together with a tightly bound water molecule are seen to be involved in the substrate specificity of UP. Enzyme activity shows a twofold dependence on potassium ion concentration. The presence of a potassium ion at the monomer/monomer interface induces some local rearrangement, which results in dimer stabilisation. The conservation of key residues and interactions with substrate in the phosphate and ribose binding pockets suggest that ribooxocarbenium ion formation during catalysis of UP may be similar to that proposed for E.coli PNP.
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{{ABSTRACT_PUBMED_15003451}}
==About this Structure==
==About this Structure==
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[[Category: Pentosyltransferase]]
[[Category: Pentosyltransferase]]
[[Category: Uridine phosphorylase]]
[[Category: Uridine phosphorylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:36:30 2008''

Revision as of 04:36, 29 July 2008

Image:1t0u.png

Template:STRUCTURE 1t0u

Crystal structure of E.coli uridine phosphorylase at 2.2 A resolution (Type-A Native)

Template:ABSTRACT PUBMED 15003451

About this Structure

1T0U is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1lgg. Full crystallographic information is available from OCA.

Reference

Crystal structures of Escherichia coli uridine phosphorylase in two native and three complexed forms reveal basis of substrate specificity, induced conformational changes and influence of potassium., Caradoc-Davies TT, Cutfield SM, Lamont IL, Cutfield JF, J Mol Biol. 2004 Mar 19;337(2):337-54. PMID:15003451

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